The domain within your query sequence starts at position 1017 and ends at position 1120; the E-value for the AP4E_app_platf domain shown below is 4.2e-51.
This domain is found in the C-terminal of the AP-4 complex subunit epsilon-1 (AP4E1). Epsilon-1 is a subunit of novel type of clathrin- or non-clathrin-associated protein coat involved in targeting proteins from the trans-Golgi network (TGN) to the endosomal-lysosomal system [ (PUBMED:11409905) (PUBMED:20972249) ].
Family alignment:
There are 368 AP4E_app_platf domains in 368 proteins in SMART's nrdb database.
Click on the following links for more information.
Evolution (species in which this domain is found)
Taxonomic distribution of proteins containing AP4E_app_platf domain.
This tree includes only several representative species. The complete taxonomic breakdown of all proteins with AP4E_app_platf domain is also avaliable.
Click on the protein counts, or double click on taxonomic names to display all proteins containing AP4E_app_platf domain in the selected taxonomic class.
Literature (relevant references for this domain)
Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.
Similar subunit interactions contribute to assembly of clathrin adaptor complexesand COPI complex: analysis using yeast three-hybrid system.
Biochem Biophys Res Commun. 2001; 284: 1083-9
Display abstract
Clathrin adaptor protein (AP) complexes are heterotetramers composed of twolarge, one medium, and one small subunits. By exploiting the yeast three-hybridsystem, we have found that an interaction between the two large subunits of theAP-1 complex, gamma-adaptin and beta1-adaptin, is markedly enhanced in thepresence of the small subunit, sigma1. Similarly, two large subunits of the AP-4 complex, epsilon-adaptin and beta4-adaptin, are found to interact with each otheronly in the presence of the small subunit, sigma4. Furthermore, we have foundthat an interaction between two large subunits of the COPI F subcomplex,gamma-COP and beta-COP, is detectable only in the presence of zeta-COP. Becausethese COPI subunits have common ancestral origins to the corresponding APsubunits, these three-hybrid data, taken together with the previous two-hybriddata, suggest that the AP complexes and the COPI F subcomplex assemble by virtue of similar subunit interactions.
Links (links to other resources describing this domain)
